ID A0A1Y2LPP7_EPING Unreviewed; 464 AA.
AC A0A1Y2LPP7;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=AAA+ ATPase domain-containing protein {ECO:0000259|SMART:SM00382};
GN ORFNames=B5807_10178 {ECO:0000313|EMBL:OSS45502.1};
OS Epicoccum nigrum (Soil fungus) (Epicoccum purpurascens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Didymellaceae; Epicoccum.
OX NCBI_TaxID=105696 {ECO:0000313|EMBL:OSS45502.1, ECO:0000313|Proteomes:UP000193240};
RN [1] {ECO:0000313|EMBL:OSS45502.1, ECO:0000313|Proteomes:UP000193240}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ICMP 19927 {ECO:0000313|EMBL:OSS45502.1,
RC ECO:0000313|Proteomes:UP000193240};
RA Fokin M., Fleetwood D., Weir B.S., Villas-Boas S.G.;
RT "Genome sequence of the saprophytic ascomycete Epicoccum nigrum ICMP 19927
RT strain isolated from New Zealand.";
RL Genome Announc. 0:0-0(2017).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the AAA ATPase family.
CC {ECO:0000256|ARBA:ARBA00006914, ECO:0000256|RuleBase:RU003651}.
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DR EMBL; KZ107854; OSS45502.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y2LPP7; -.
DR STRING; 105696.A0A1Y2LPP7; -.
DR InParanoid; A0A1Y2LPP7; -.
DR OMA; QDDTDPM; -.
DR OrthoDB; 1707207at2759; -.
DR Proteomes; UP000193240; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0008540; C:proteasome regulatory particle, base subcomplex; IEA:UniProt.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR CDD; cd19502; RecA-like_PAN_like; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR041569; AAA_lid_3.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR003960; ATPase_AAA_CS.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR032501; Prot_ATP_ID_OB_2nd.
DR PANTHER; PTHR23073; 26S PROTEASOME REGULATORY SUBUNIT; 1.
DR PANTHER; PTHR23073:SF24; 26S PROTEASOME REGULATORY SUBUNIT 4; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF17862; AAA_lid_3; 1.
DR Pfam; PF16450; Prot_ATP_ID_OB_C; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS00674; AAA; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU003651};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU003651};
KW Proteasome {ECO:0000256|ARBA:ARBA00022942};
KW Reference proteome {ECO:0000313|Proteomes:UP000193240}.
FT DOMAIN 242..381
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 96..129
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 15..31
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 112..126
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 464 AA; 51338 MW; 9C7E695C3D6693F9 CRC64;
MGNQQSSAGG GGAPGDDKSK KDKKEKPKYE PPPQPTTRIG RKKKKQAGPS AAAKLPAVYP
TARCKLRYLR MQRIHDHLLL EEEYVENQER IRKAKAVKEG AGPVNVNASP EESDRNADER
SRVDDMRGSP MGVGNLEELI DDDHAIVSSA TGPEYYVSIM SFVDKDLLEP GASILLHHKS
VSVVGVLTDD ADPLVSTMKI DKAPTESYAD IGGLETQIQE VREAVELPLL HPELYEEMGI
KPPKGVILYG APGTGKTLLA KAVANQTSAT FLRIVGSELI QKYLGDGPRL VRQLFQTAAE
NAPSIVFIDE IDAIGTKRYE STSGGEREIQ RTMLELLNQL DGFDDRGDIK VIMATNKIDT
LDPALIRPGR IDRKILFENP DQHTKKKIFT LHTSKMSLNE DVDLDEFINQ KDDLSGADIK
AICSEAGLLA LRERRMRVQM DDFRQARERV LKTKSEGEPE GLYL
//
